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Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms
In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers. In this study, we analyzed conformational stabilities of the recombinant bOBP and its mono...
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| Gepubliceerd in: | PeerJ |
|---|---|
| Hoofdauteurs: | , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
PeerJ Inc.
2016
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4841237/ https://ncbi.nlm.nih.gov/pubmed/27114857 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7717/peerj.1574 |
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